TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of three myotoxic phospholipases A2 from Bothrops brazili venom
AU - Fernandes, Carlos A.H.
AU - Gartuzo, Elaine C.G.
AU - Pagotto, Ivan
AU - Comparetti, Edson J.
AU - Huancahuire-Vega, Salomón
AU - Ponce-Soto, Luis Alberto
AU - Costa, Tássia R.
AU - Marangoni, Sergio
AU - Soares, Andreimar M.
AU - Fontes, Marcos R.M.
PY - 2012/8
Y1 - 2012/8
N2 - Two myotoxic and noncatalytic Lys49-phospholipases A2 (braziliantoxin-II and MT-II) and a myotoxic and catalytic phospholipase A2 (braziliantoxin-III) from the venom of the Amazonian snake Bothrops brazili were crystallized. The crystals diffracted to resolutions in the range 2.56-2.05 Å and belonged to space groups P3121 (braziliantoxin-II), P6522 (braziliantoxin-III) and P21 (MT-II). The structures were solved by molecular-replacement techniques. Both of the Lys49-phospholipases A2 (braziliantoxin-II and MT-II) contained a dimer in the asymmetric unit, while the Asp49-phospholipase A2 braziliantoxin-III contained a monomer in its asymmetric unit. Analysis of the quaternary assemblies of the braziliantoxin-II and MT-II structures using the PISA program indicated that both models have a dimeric conformation in solution. The same analysis of the braziliantoxin-III structure indicated that this protein does not dimerize in solution and probably acts as a monomer in vivo, similar to other snake-venom Asp49-phospholipases A2.
AB - Two myotoxic and noncatalytic Lys49-phospholipases A2 (braziliantoxin-II and MT-II) and a myotoxic and catalytic phospholipase A2 (braziliantoxin-III) from the venom of the Amazonian snake Bothrops brazili were crystallized. The crystals diffracted to resolutions in the range 2.56-2.05 Å and belonged to space groups P3121 (braziliantoxin-II), P6522 (braziliantoxin-III) and P21 (MT-II). The structures were solved by molecular-replacement techniques. Both of the Lys49-phospholipases A2 (braziliantoxin-II and MT-II) contained a dimer in the asymmetric unit, while the Asp49-phospholipase A2 braziliantoxin-III contained a monomer in its asymmetric unit. Analysis of the quaternary assemblies of the braziliantoxin-II and MT-II structures using the PISA program indicated that both models have a dimeric conformation in solution. The same analysis of the braziliantoxin-III structure indicated that this protein does not dimerize in solution and probably acts as a monomer in vivo, similar to other snake-venom Asp49-phospholipases A2.
KW - Bothrops brazili
KW - MT-II
KW - braziliantoxin-II
KW - braziliantoxin-III
KW - phospholipases A2
UR - http://www.scopus.com/inward/record.url?scp=84864866373&partnerID=8YFLogxK
U2 - 10.1107/S1744309112026073
DO - 10.1107/S1744309112026073
M3 - Article
C2 - 22869126
AN - SCOPUS:84864866373
SN - 1744-3091
VL - 68
SP - 935
EP - 938
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 8
ER -